Structural basis for plant-specific type III polyketide synthase based on the X-ray crystal structure analysis and computational chemistry
Project/Area Number |
24710246
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Living organism molecular science
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Research Institution | University of Toyama |
Principal Investigator |
MORITA Hiroyuki 富山大学, 和漢医薬学総合研究所, 教授 (20416663)
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Project Period (FY) |
2012-04-01 – 2014-03-31
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Project Status |
Completed (Fiscal Year 2013)
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Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
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Keywords | 生合成 / ポリケタイド合成酵素 / 酵素工学 / ポリフェノール / アルカロイド / ポリケタイド / 閉環酵素 / X線結晶構造解析 / 結晶構造解析 |
Research Abstract |
We solved crystal structure of an octaketide synthase (OKS) F66L/N222G mutant enzyme that catalyzes the longest number of malonyl-CoA condensations to produce TW95a. Furthermore, we succeeded in producing an OKS mutant enzyme that increased enzyme activity for the formation of TW95a to approximately 1.5 times on the basis of the crystal structure. In addition, we succeeded in cloning a novel type III PKS that specifically catalyzes the formation of quinolinone.
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Report
(3 results)
Research Products
(50 results)
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[Journal Article] Cloning and structure-function analyses of quinolone- and acridone-producing novel type III polyketide synthases from Citrus microcarpa2013
Author(s)
Mori, T., Shimokawa, Y., Matsui, T., Kinjo, K., Kato, R., Noguchi, H., Sugio, S., Morita, H., Abe, I.
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Journal Title
J. Biol. Chem.
Volume: 288
Issue: 40
Pages: 28845-28858
DOI
Related Report
Peer Reviewed
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